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蛋白质SUMO化的生化分析。

Biochemical analysis of protein SUMOylation.

作者信息

Alontaga Aileen Y, Bobkova Ekaterina, Chen Yuan

机构信息

Department of Molecular Medicine, Beckman Research Institute of the City of Hope, Duarte, California, USA.

出版信息

Curr Protoc Mol Biol. 2012 Jul;Chapter 10:Unit10.29. doi: 10.1002/0471142727.mb1029s99.

DOI:10.1002/0471142727.mb1029s99
PMID:22870855
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3477621/
Abstract

SUMOylation, the covalent attachment of Small Ubiquitin-like MOdifier (SUMO) polypeptides to other proteins, is among the most important post-translational modifications that regulate the functional properties of a large number of proteins. SUMOylation is broadly involved in cellular processes such as gene transcription, hormone response, signal transduction, DNA repair, and nuclear transport. SUMO modification has also been implicated in the pathogenesis of human diseases, such as cancer, neurodegenerative disorders, and viral infection. Attachment of a SUMO protein to another protein is carried out in multiple steps catalyzed by three enzymes. This unit describes and discusses the in vitro biochemical methods used for investigating each step of the SUMOylation process. In addition, a high-throughput screening protocol is included for the identification of inhibitors of SUMOylation.

摘要

SUMO化是指小泛素样修饰物(SUMO)多肽与其他蛋白质的共价连接,是调节大量蛋白质功能特性的最重要的翻译后修饰之一。SUMO化广泛参与细胞过程,如基因转录、激素反应、信号转导、DNA修复和核运输。SUMO修饰也与人类疾病的发病机制有关,如癌症、神经退行性疾病和病毒感染。SUMO蛋白与另一种蛋白质的连接是由三种酶催化的多个步骤完成的。本单元描述并讨论了用于研究SUMO化过程各个步骤的体外生化方法。此外,还包括一个用于鉴定SUMO化抑制剂的高通量筛选方案。

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引用本文的文献

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Allosteric Inhibition of Ubiquitin-like Modifications by a Class of Inhibitor of SUMO-Activating Enzyme.一类 SUMO 激活酶抑制剂对泛素样修饰的别构抑制。
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Sumoylation of RORγt regulates T17 differentiation and thymocyte development.SUMOylation 修饰调控 RORγt 转录因子的 T17 细胞分化和胸腺细胞发育。
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Control of regional decidualization in implantation: Role of FoxM1 downstream of Hoxa10 and cyclin D3.着床过程中局部蜕膜化的调控:Hoxa10和细胞周期蛋白D3下游的FoxM1的作用
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An electrophoretic mobility shift assay identifies a mechanistically unique inhibitor of protein sumoylation.一种电泳迁移率变动分析鉴定出一种蛋白质类泛素化修饰的独特作用机制抑制剂。
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RNF4-dependent hybrid SUMO-ubiquitin chains are signals for RAP80 and thereby mediate the recruitment of BRCA1 to sites of DNA damage.RNF4 依赖性杂合 SUMO-泛素链是 RAP80 的信号,从而介导 BRCA1 招募到 DNA 损伤部位。
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本文引用的文献

1
Entropy-driven mechanism of an E3 ligase.熵驱动的 E3 连接酶机制。
Biochemistry. 2011 Jun 28;50(25):5757-66. doi: 10.1021/bi2001856. Epub 2011 Jun 3.
2
The SUMOylation of matrix protein M1 modulates the assembly and morphogenesis of influenza A virus.基质蛋白 M1 的 SUMOylation 调节甲型流感病毒的组装和形态发生。
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SUMO-interacting motifs of human TRIM5α are important for antiviral activity.SUMO-interacting motifs of human TRIM5α are important for antiviral activity. 人源 TRIM5α 的 SUMO 相互作用基序对于抗病毒活性很重要。
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SUMO and its role in human diseases.SUMO 及其在人类疾病中的作用。
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Influenza A virus interacts extensively with the cellular SUMOylation system during infection.甲型流感病毒在感染过程中与细胞 SUMOylation 系统广泛相互作用。
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MDA5 is SUMOylated by PIAS2β in the upregulation of type I interferon signaling.MDA5 通过 PIAS2β 的 SUMOylation 在 I 型干扰素信号的上调中起作用。
Mol Immunol. 2011 Jan;48(4):415-22. doi: 10.1016/j.molimm.2010.09.003. Epub 2010 Dec 14.
7
Huntington's disease is a disorder of the corpus striatum: focus on Rhes (Ras homologue enriched in the striatum).亨廷顿病是纹状体的一种疾病:聚焦于 Rhes(富含在纹状体中的 Ras 同源物)。
Neuropharmacology. 2011 Jun;60(7-8):1187-92. doi: 10.1016/j.neuropharm.2010.10.025. Epub 2010 Oct 31.
8
Transcriptional repression by sumoylation of Epstein-Barr virus BZLF1 protein correlates with association of histone deacetylase.BZLF1 蛋白的 SUMO 化转录抑制与组蛋白去乙酰化酶的关联有关。
J Biol Chem. 2010 Jul 30;285(31):23925-35. doi: 10.1074/jbc.M109.095356. Epub 2010 Jun 1.
9
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J Biol Chem. 2010 Jul 30;285(31):23732-8. doi: 10.1074/jbc.M110.114660. Epub 2010 May 25.
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Mechanisms, regulation and consequences of protein SUMOylation.蛋白质SUMO化修饰的机制、调控及后果
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